Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [Cleaved into: Non-structural protein 1 (nsp1) (p28); Non-structural protein 2 (nsp2) (p65); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.69) (PL1-PRO/PL2-PRO) (PL1/PL2) (Papain-like proteinases 1/2) (p210); Non-structural protein 4 (nsp4) (Peptide HD2) (p44); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (M-PRO) (nsp5) (p27); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7) (p10); Non-structural protein 8 (nsp8) (p22); Non-structural protein 9 (nsp9) (p12); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL) (p15); Non-structural protein 11 (nsp11)]

 R1A_CVM2                Reviewed;        4416 AA.
P0C6U9; Q9PYA3;
10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
10-JUN-2008, sequence version 1.
23-MAY-2018, entry version 63.
RecName: Full=Replicase polyprotein 1a;
Short=pp1a;
AltName: Full=ORF1a polyprotein;
Contains:
RecName: Full=Non-structural protein 1;
Short=nsp1;
AltName: Full=p28;
Contains:
RecName: Full=Non-structural protein 2;
Short=nsp2;
AltName: Full=p65;
Contains:
RecName: Full=Non-structural protein 3;
Short=nsp3;
EC=3.4.19.12;
EC=3.4.22.69;
AltName: Full=PL1-PRO/PL2-PRO;
AltName: Full=PL1/PL2;
AltName: Full=Papain-like proteinases 1/2;
AltName: Full=p210;
Contains:
RecName: Full=Non-structural protein 4;
Short=nsp4;
AltName: Full=Peptide HD2;
AltName: Full=p44;
Contains:
RecName: Full=3C-like proteinase;
Short=3CL-PRO;
Short=3CLp;
EC=3.4.22.-;
AltName: Full=M-PRO;
AltName: Full=nsp5;
AltName: Full=p27;
Contains:
RecName: Full=Non-structural protein 6;
Short=nsp6;
Contains:
RecName: Full=Non-structural protein 7;
Short=nsp7;
AltName: Full=p10;
Contains:
RecName: Full=Non-structural protein 8;
Short=nsp8;
AltName: Full=p22;
Contains:
RecName: Full=Non-structural protein 9;
Short=nsp9;
AltName: Full=p12;
Contains:
RecName: Full=Non-structural protein 10;
Short=nsp10;
AltName: Full=Growth factor-like peptide;
Short=GFL;
AltName: Full=p15;
Contains:
RecName: Full=Non-structural protein 11;
Short=nsp11;
ORFNames=1a;
Murine coronavirus (strain 2) (MHV-2) (Murine hepatitis virus).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Nidovirales; Coronaviridae; Coronavirinae; Betacoronavirus.
NCBI_TaxID=76344;
NCBI_TaxID=10090; Mus musculus (Mouse).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
Das Sarma J., Hingley S.T., Lai M.M.C., Weiss S.R., Lavi E.;
"Pathogenesis and sequence analysis of mouse hepatitis virus type 2:
an experimental model system of acute meningitis and hepatitis in
mice.";
Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: The papain-like proteinase 1 (PL1-PRO) and papain-like
proteinase 2 (PL2-PRO) are responsible for the cleavages located
at the N-terminus of the replicase polyprotein. In addition, PLP2
possesses a deubiquitinating/deISGylating activity and processes
both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from
cellular substrates. Antagonizes innate immune induction of type I
interferon by blocking the phosphorylation, dimerization and
subsequent nuclear translocation of host IRF-3 (By similarity).
{ECO:0000250}.
-!- FUNCTION: The main proteinase 3CL-PRO is responsible for the
majority of cleavages as it cleaves the C-terminus of replicase
polyprotein at 11 sites. Recognizes substrates containing the core
sequence [ILMVF]-Q-|-[SGACN]. Inhibited by the substrate-analog
Cbz-Val-Asn-Ser-Thr-Leu-Gln-CMK. Also contains an ADP-ribose-1''-
phosphate (ADRP)-binding function (By similarity).
{ECO:0000255|PROSITE-ProRule:PRU00772}.
-!- FUNCTION: Nsp7-nsp8 hexadecamer may possibly confer processivity
to the polymerase, maybe by binding to dsRNA or by producing
primers utilized by the latter. {ECO:0000250}.
-!- FUNCTION: Nsp9 is a ssRNA-binding protein. {ECO:0000250}.
-!- FUNCTION: Non-structural protein 1: binds to the 40S ribosomal
subunit and inhibits host translation. The nsp1-40S ribosome
complex further induces an endonucleolytic cleavage near the 5'UTR
of host mRNAs, targeting them for degradation. By suppressing host
gene expression, nsp1 facilitates efficient viral gene expression
in infected cells and evasion from host immune response (By
similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: TSAVLQ-|-SGFRK-NH(2) and SGVTFQ-|-GKFKK the
two peptides corresponding to the two self-cleavage sites of the
SARS 3C-like proteinase are the two most reactive peptide
substrates. The enzyme exhibits a strong preference for substrates
containing Gln at P1 position and Leu at P2 position.
-!- CATALYTIC ACTIVITY: Thiol-dependent hydrolysis of ester,
thioester, amide, peptide and isopeptide bonds formed by the C-
terminal Gly of ubiquitin (a 76-residue protein attached to
proteins as an intracellular targeting signal).
-!- SUBUNIT: 3CL-PRO exists as monomer and homodimer. Eight copies of
nsp7 and eight copies of nsp8 assemble to form a
heterohexadecamer. Nsp9 is a dimer. Nsp10 forms a dodecamer (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Non-structural protein 3: Host membrane
{ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Non-structural protein 4: Host membrane
{ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Non-structural protein 6: Host membrane
{ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Non-structural protein 7: Host cytoplasm,
host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and
nsp10 are localized in cytoplasmic foci, largely perinuclear. Late
in infection, they merge into confluent complexes (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Non-structural protein 8: Host cytoplasm,
host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and
nsp10 are localized in cytoplasmic foci, largely perinuclear. Late
in infection, they merge into confluent complexes (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Non-structural protein 9: Host cytoplasm,
host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and
nsp10 are localized in cytoplasmic foci, largely perinuclear. Late
in infection, they merge into confluent complexes (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Non-structural protein 10: Host cytoplasm,
host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and
nsp10 are localized in cytoplasmic foci, largely perinuclear. Late
in infection, they merge into confluent complexes (By similarity).
{ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Ribosomal frameshifting; Named isoforms=2;
Name=Replicase polyprotein 1a; Synonyms=pp1a, ORF1a polyprotein;
IsoId=P0C6U9-1; Sequence=Displayed;
Note=Produced by conventional translation.;
Name=Replicase polyprotein 1ab; Synonyms=pp1ab;
IsoId=P0C6X8-1; Sequence=External;
Note=Produced by -1 ribosomal frameshifting at the 1a-1b genes
boundary.;
-!- DOMAIN: The hydrophobic domains (HD) could mediate the membrane
association of the replication complex and thereby alter the
architecture of the host cell membrane.
-!- PTM: Specific enzymatic cleavages in vivo by its own proteases
yield mature proteins. 3CL-PRO and PL-PRO proteinases are
autocatalytically processed (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the coronaviruses polyprotein 1ab family.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AF201929; AAF19383.1; -; Genomic_RNA.
ProteinModelPortal; P0C6U9; -.
SMR; P0C6U9; -.
PRIDE; P0C6U9; -.
Proteomes; UP000139707; Genome.
GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
GO; GO:0044220; C:host cell perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
GO; GO:0008242; F:omega peptidase activity; IEA:InterPro.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:InterPro.
GO; GO:0036459; F:thiol-dependent ubiquitinyl hydrolase activity; IEA:UniProtKB-EC.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0039595; P:induction by virus of catabolism of host mRNA; IEA:UniProtKB-KW.
GO; GO:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW.
GO; GO:0039648; P:modulation by virus of host protein ubiquitination; IEA:UniProtKB-KW.
GO; GO:0039548; P:suppression by virus of host IRF3 activity; IEA:UniProtKB-KW.
GO; GO:0039579; P:suppression by virus of host ISG15 activity; IEA:UniProtKB-KW.
GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
GO; GO:0019079; P:viral genome replication; IEA:InterPro.
GO; GO:0019082; P:viral protein processing; IEA:InterPro.
Gene3D; 1.10.150.420; -; 1.
Gene3D; 1.10.8.370; -; 1.
Gene3D; 2.40.10.250; -; 1.
Gene3D; 3.10.20.350; -; 1.
InterPro; IPR022570; B-CoV_NSP1.
InterPro; IPR032505; Corona_NSP4_C.
InterPro; IPR002589; Macro_dom.
InterPro; IPR032592; NAR_dom.
InterPro; IPR036333; NSP10_sf.
InterPro; IPR038123; NSP4_C_sf.
InterPro; IPR014828; NSP7.
InterPro; IPR037204; NSP7_sf.
InterPro; IPR014829; NSP8.
InterPro; IPR037230; NSP8_sf.
InterPro; IPR014822; NSP9.
InterPro; IPR036499; NSP9_sf.
InterPro; IPR002705; Pept_C30/C16_B_coronavir.
InterPro; IPR008740; Peptidase_C30.
InterPro; IPR013016; Peptidase_C30/C16.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR038083; pp1a/1ab.
InterPro; IPR018995; RNA_synth_NSP10_coronavirus.
InterPro; IPR029063; SAM-dependent_MTases.
InterPro; IPR014827; Viral_protease.
Pfam; PF16348; Corona_NSP4_C; 1.
Pfam; PF11963; DUF3477; 1.
Pfam; PF01661; Macro; 1.
Pfam; PF16251; NAR; 1.
Pfam; PF09401; NSP10; 1.
Pfam; PF08716; nsp7; 1.
Pfam; PF08717; nsp8; 1.
Pfam; PF08710; nsp9; 1.
Pfam; PF01831; Peptidase_C16; 1.
Pfam; PF05409; Peptidase_C30; 1.
Pfam; PF08715; Viral_protease; 1.
SMART; SM00506; A1pp; 1.
SUPFAM; SSF101816; SSF101816; 1.
SUPFAM; SSF140367; SSF140367; 1.
SUPFAM; SSF143076; SSF143076; 1.
SUPFAM; SSF144246; SSF144246; 1.
SUPFAM; SSF159936; SSF159936; 1.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF53335; SSF53335; 1.
PROSITE; PS51442; M_PRO; 1.
PROSITE; PS51154; MACRO; 1.
PROSITE; PS51124; PEPTIDASE_C16; 2.
3: Inferred from homology;
Activation of host autophagy by virus; Complete proteome;
Decay of host mRNAs by virus;
Eukaryotic host gene expression shutoff by virus;
Eukaryotic host translation shutoff by virus; Host cytoplasm;
Host gene expression shutoff by virus; Host membrane;
Host mRNA suppression by virus; Host-virus interaction; Hydrolase;
Inhibition of host innate immune response by virus;
Inhibition of host interferon signaling pathway by virus;
Inhibition of host IRF3 by virus; Inhibition of host ISG15 by virus;
Inhibition of host RLR pathway by virus; Membrane; Metal-binding;
Modulation of host ubiquitin pathway by viral deubiquitinase;
Modulation of host ubiquitin pathway by virus; Protease;
Reference proteome; Repeat; Ribosomal frameshifting; RNA-binding;
Thiol protease; Transmembrane; Transmembrane helix;
Ubl conjugation pathway; Viral immunoevasion; Zinc; Zinc-finger.
CHAIN 1 4416 Replicase polyprotein 1a.
/FTId=PRO_0000338266.
CHAIN 1 247 Non-structural protein 1. {ECO:0000250}.
/FTId=PRO_0000338267.
CHAIN 248 832 Non-structural protein 2. {ECO:0000250}.
/FTId=PRO_0000338268.
CHAIN 833 2783 Non-structural protein 3. {ECO:0000250}.
/FTId=PRO_0000338269.
CHAIN 2784 3279 Non-structural protein 4. {ECO:0000250}.
/FTId=PRO_0000338270.
CHAIN 3280 3582 3C-like proteinase. {ECO:0000250}.
/FTId=PRO_0000338271.
CHAIN 3583 3869 Non-structural protein 6. {ECO:0000250}.
/FTId=PRO_0000338272.
CHAIN 3870 3961 Non-structural protein 7. {ECO:0000250}.
/FTId=PRO_0000338273.
CHAIN 3962 4155 Non-structural protein 8. {ECO:0000250}.
/FTId=PRO_0000338274.
CHAIN 4156 4265 Non-structural protein 9. {ECO:0000250}.
/FTId=PRO_0000338275.
CHAIN 4266 4402 Non-structural protein 10. {ECO:0000250}.
/FTId=PRO_0000338276.
CHAIN 4403 4416 Non-structural protein 11. {ECO:0000255}.
/FTId=PRO_0000338277.
TRANSMEM 2232 2252 Helical. {ECO:0000255}.
TRANSMEM 2260 2280 Helical. {ECO:0000255}.
TRANSMEM 2346 2366 Helical. {ECO:0000255}.
TRANSMEM 2388 2408 Helical. {ECO:0000255}.
TRANSMEM 2789 2809 Helical. {ECO:0000255}.
TRANSMEM 2869 2889 Helical. {ECO:0000255}.
TRANSMEM 3042 3062 Helical. {ECO:0000255}.
TRANSMEM 3064 3084 Helical. {ECO:0000255}.
TRANSMEM 3096 3116 Helical. {ECO:0000255}.
TRANSMEM 3123 3143 Helical. {ECO:0000255}.
TRANSMEM 3148 3168 Helical. {ECO:0000255}.
TRANSMEM 3591 3611 Helical. {ECO:0000255}.
TRANSMEM 3621 3641 Helical. {ECO:0000255}.
TRANSMEM 3647 3667 Helical. {ECO:0000255}.
TRANSMEM 3690 3710 Helical. {ECO:0000255}.
TRANSMEM 3717 3737 Helical. {ECO:0000255}.
TRANSMEM 3744 3764 Helical. {ECO:0000255}.
TRANSMEM 3788 3808 Helical. {ECO:0000255}.
DOMAIN 1031 1268 Peptidase C16 1. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
DOMAIN 1269 1429 Macro. {ECO:0000255|PROSITE-
ProRule:PRU00490}.
DOMAIN 1625 1884 Peptidase C16 2. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
DOMAIN 3280 3582 Peptidase C30. {ECO:0000255|PROSITE-
ProRule:PRU00772}.
ZN_FING 1145 1173 C4-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
ZN_FING 1741 1777 C4-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00444}.
ZN_FING 4339 4355 {ECO:0000250}.
ZN_FING 4381 4394 {ECO:0000250}.
REGION 2232 2408 HD1.
REGION 2789 3168 HD2.
REGION 3525 3808 HD3.
ACT_SITE 1068 1068 For PL1-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 1219 1219 For PL1-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 1663 1663 For PL2-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 1820 1820 For PL2-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00444}.
ACT_SITE 3320 3320 For 3CL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00772}.
ACT_SITE 3424 3424 For 3CL-PRO activity.
{ECO:0000255|PROSITE-ProRule:PRU00772}.
SITE 247 248 Cleavage; by PL1-PRO. {ECO:0000250}.
SITE 832 833 Cleavage; by PL1-PRO. {ECO:0000250}.
SITE 2783 2784 Cleavage; by PL2-PRO. {ECO:0000250}.
SITE 3279 3280 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3582 3583 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3869 3870 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 3961 3962 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 4155 4156 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 4265 4266 Cleavage; by 3CL-PRO. {ECO:0000250}.
SITE 4402 4403 Cleavage; by 3CL-PRO. {ECO:0000250}.
SEQUENCE 4416 AA; 491187 MW; 4FD965F1EEC15362 CRC64;
MAKMGKYGLG FKWAPEFPWM LPNASEKLGS PERSEEDGFC PSAAQEPKTK GKTLINHVRV
DCSRLPALEC CVQSAIIRDI FVDEDPLNVE ASTMMALQFG SAVLVKPSKR LSIQAWAKLG
VLPKTPAMGL FKRFCLCNTR ECVCDAHVAF QLFTVQPDGV CLGNGRFIGW FVPVTAIPAY
AKQWLQPWSI LLRKGGNKGS VTSGHFRRAV TMPVYDFNVE DACEEVHLNP KGKYSRKAYA
LLKGYRGVKS ILFLDQYGCD YTGRLAKGLE DYGDCTLEEM KELFPVWCDS LDNEVVVAWH
VDRDPRAVMR LQTLATIRSI GYVGQPTEDL VDGDVVVREP AHLLAANAIV KRLPRLVETM
LYTDSSVTEF CYKTKLCDCG FITQFGYVDC CGDACDFRGW VPGNMMDGFL CPGCSKSYMP
WELEAQSSGV IPKGGVLFTQ STDTVNRESF KLYGHAVVPF GSAVYWSPYP GMWLPVIWSS
VKSYADLTYT GVVGCKAIVQ ETDAICRSLY MDYVQHKCGN LEQRAILGLD DVYHRQLLVN
RGDYSLLLEN VDLFVKRRAE FACKFATCGD GLVPLLLDGL VPRSYYLIKS GQAFTSMMVN
FSHEVTDMCM DMALLFMHDV KVATKYVKKV TGKLAVRFKA LGVAVVRKIT EWFDLAVDTA
ASAAGWLCYQ LVNGLFAVAN GGITFLSDVP ELVKNFVDKF KVFFKVLIDS MSVSVLSGLT
VVKTASNRVC LAGCKVYEVV QKRLSAYVMP VGCNEATCLV GEIEPAVVED DVVDVVKAPL
TYQGCCKPPT SFEKICVVDK LYMAKCGDQF YPVVVDNDTI GVLDQCWRFP CAGKKVEFND
KPKVKEIPST RKIKINFALD ATFDSVLSKA CSEFEVDKDV TLDELLDVVL DAVESTLSPC
KEHDVIGTKV CALLNRLAED YVYLFDEGGE EVIAPKMYCS FSAPDDEDCV AADVVDADEN
QGDDADDSAA LVTDTQEEDG VAKGQVGVAE SDARLDQVEA FDIEKVEDPI LNELSAELNA
PADKTYEDVL AFDAIYSEAL SAFYAVPGDE THFKVCGFYS PAIERTNCWL RSTLIVMQSL
PLEFKDLEMQ KLWLSYKSSY NKEFVDKLVK SVPKSIILPQ GGYVADFAYF FLSQCSFKAY
ANWRCLKCDM DLKLQGLDAM FFYGDVVSHV CKCGTGMTLL SADIPYTLHF GLRDDKFCAF
YTPRKVFRAA CVVDVNDCHS MAVVDGKQID GKVVTKFNGD KYDFMVGHGM AFSMSAFEIA
QLYGSCITPN VCFVKGDVIK VLRRVGAEVI VNPANGRMAH GAGVAGAIAK AAGKSFIKET
ADMVKNQGVC QVGECYESTG GNLCKTVLNI VGPDARGHGK QCYSFLERAY QHINKCDDVV
TTLISAGIFS VPTDVSLTYL IGVVTKNVIL VSNNKDDFDV IEKCQVTSIA GTKALSLQLA
KNLCRDVKFE TNACDSLFSD SCFVSSYDVL QEVELLRHDI QLDDDARVFV QAHMDNLPAD
WRLVNKFDSV DGVRTVKYFE CPGEIFVSSQ GKKFGYVQNG SFKVASVSQI RALLANKVDV
LCTVDGVNFR SCCVAEGEVF GKTLGSVFCD GINVTKVRCS AIHKGKVFFQ YSGLSAADLV
AVTDAFGFDE PQLLKYYNML GMCKWPVVVC GNYFAFKQSN NNCYINVACL MLQHLSLKFH
KWQWQEAWNE FRSGKPLRFV SLVLAKGSFK FNEPSDSTDF MRVVLREADL SGATCDFEFV
CKCGVKQEQR KGVDAVMHFG TLDKGDLAKG YTIACTCGNK LVHCTQLNVP FLICSNKPEG
KKLPDDVVAA NIFTGGSLGH YTHVKCKPKY QLYDACNVSK VSEAKGNFTD CLYLKNLKQT
FSSKLTTFYL DDVKCVEYNP DLSQYYCESG KYYTKPIIKA QFRTFEKVEG VYTNFKLVGH
SIAEKFNAKL GFDCNSPFTE YKITEWPTAT GDVVLASDDL YVSRYSGGCV TFGKPVIWLG
HEEASLKSLT YFNRPSVVCE NKFNVLPVDV SEPTDKGPVP AAVLVTGALS GAATAPGTAK
EQKVCASDSV VDQVVSGFLS DLSGATVDVK EVKLNGVKKP IKVEDSVVVN DPTSETKVVK
SLSIVDVYDM FLTGCRYVVW MANELSRLVN SPTVREYVKW GMTKIVIPAK LVLLRDEKQE
FVAPKVVKAK VIACYSAVKW FFLYCFSWIK FNTDNKVIYT TEVASKLTFN LCCLAFKNAL
QTFNWNVVSR GFFLVATVFL LWFNFLYANV ILSDFYLPNI GFFPTFVGQI VAWVKTTFGI
FTLCDLYQVS DVGYRSSFCN GSMVCELCFS GFDMLDNYDA INVVQHVVDR RVSFDYISLF
KLVVELVIGY SLYTVCFYPL FGLIGMQLLT TWLPEFFMLE TMHWSARFFV FVANMLPAFT
LLRFYIVVTA MYKIFCLCRH VMYGCSRPGC LFCYKRNRSV RVKCSTVVGG TLRYYDVMAN
GGTGFCAKHQ WNCLNCSAFG PGNTFITHEA AADLSKELKR PVNPTDSAYY LVTEVKQVGC
SMRLFYERDG QRVYDDVSAS LFVDMNGLLH SKVKGVPETH VVVVENEADK AGFLNAAVFY
AQSLYRPMLL VEKKLITTAN TGLSVSQTMF DLYVDSLLGV LDVDRKSLTS FVNAAHNSLK
EGVQLEQVMD TFIGCARRKC AIDSDVETKS ITKSIMSAVN AGVDFTDESC NNLVPTYVKS
DTIVAADLGV LIQNNAKHVQ ANVAKAANVA CIWSVDAFNQ LSADLQHRLR KACSKTGLKI
KLTYNKQEAN VPILTTPFSL KGGAVFSKVL QWLFVVNLIC FIVLWALMPT YAVHKSDMQL
PLYASFKVID NGVLRDVTVT DACFANKFIQ FDQWYESTFG LVYYRNSRAC PVVVAVIDQD
IGYTLFNVPT KVLRYGFHVL HFITHAFATD SVQCYTPHMQ IPYDNFYASG CVLSSLCTML
AHADGTPHPY CYTEGIMHNA SLYDSLAPHV RYNLANSNGY IRFPEVVSEG IVRIVRTRSM
TYCRVGLCED AEEGVCFNFN SSWVLNNPYY RAMPGTFCGR NAFDLIHQVL GGLVRPIDFF
ALTASSVAGA ILAIIVVLAF YYLIKLKRAF GDYTSVVVIN VIVWCINFLM LFVFQVYPTL
SCLYACFYFY TTLYFPSEIS VVMHLQWLVM YGAIMPLWFC IIYVAVVVSN HALWLFSYCR
KLGTEVRSDG TFEEMSLTTF MITKESYCKL KNSVSDVAFN RYLSLYNKYR YFSGKMDTAA
YREAACSQLA KAMETFNHNN GNDVLYQPPT ASVTTSFLQS GIVKMVFPTS KVEPCVVSVT
YGNMTLNGLW LDDKVYCPRH VICSSADMTD PDYSNLLCRV ISSDFCVMSG RMSLTVMSYQ
MQGSLLVLTV TLQNPNTPKY SFGVVKPGET FTVLAAYNGK SQGAFHVTMR SSYTIKGSFL
CGSCGSVGYV LTGDSVRFVY MHQLELSTGC HTGTDFSGNF YGPYRDAQVV QLPVQDYTQT
VNVVAWLYAA ILNRCNWFVQ SDSCSLEEFN VWAMTNGFSS IKADLVLDAL ASMTGVTVEQ
ILAAIKRLYS GFQGKQILGS CVLEDELTPS DVYQQLAGVK LQSKRTRVVK GTCCWILAST
LLFCSIISAF VKWTMFMYVT THMLGVTLCA LCFVSFAMLL VKHKHLYLTM FIMPVLCTLF
YTNYLVVYKQ SFRGLAYAWL SHFVPAVDYT YMDEVLYGVV LLVAMVFVTM RSINHDVFSV
MFLVGRLVSL VSMWYFGANL EEEVLLFLTS LFGTYTWTTM LSLATAKVIA KWLAVNVLYF
TDVPQVKLVL LSYLCIGYVC CCYWGVLSLL NSIFRMPLGV YNYKISVQEL RYMNANGLRP
PRNSFEALVL NFKLLGIGGV PVIEVSQIQS RLTDVKCVNV VLLNCLQHLH IASSSKLWQY
CSTLHNEILA TSDLSVAFDK LAQLLVVLFA NPAAVDSKCL ASIEEVSDDY VRDSTVLQAL
QSEFVNMASF VEYELAKKNL DEAKASGSAN QQQIKQLEKA CNIAKSAYER DRAVARKLER
MADLALTNMY KEARINDKKS KVVSALQTML FSMIRKLDNQ ALNSILDNAV KGCVPLNAIP
SLTSNTLTII VPDKQVFDQV VDNVYVTYAG NVWHIQSIQD ADGAVKQLNE IDVNITWPLV
IAANRHNEVS SVVLQNNELM PQKLRTQVVN SGSDMNCNTP TQCYYNTTGM GKIVYAILSD
CDGLKYTKIV KEDGNCVVLE LDPPCKFSVQ DVKGLKIKYL YFVKGCNTLA RGWVVGTLSS
TVRLQAGTAT EYASNSAIRS LCAFSVDPKK TYLDYIQQGG APVTNCVKML CDHAGTGMAI
TIKPEATTNQ DSYGGASVCI YCRSRVEHPD VDGLCKLRGK FVQVPLGIKD PVSYVLTHDV
CQVCGFWRDG SCSCVGTGSQ FQSKDTNFLN GFGVQV


Related products :

Catalog number Product name Quantity
orb81767 Measles Virus Non-Structural C-Protein (1-51) protein The E.coli derived recombinant protein contains the Non-Structural C-Protein immunodominant regions, 1-51 amino acids. For research use only. 100
10-663-45517 Measles Virus Non-Structural C-Protein (MEVNSCP) - Protein P; Non-structural protein C. 38 kDa_29 kDa N_A 1 mg
10-663-45517 Measles Virus Non-Structural C-Protein (MEVNSCP) - Protein P; Non-structural protein C. 38 kDa_29 kDa N_A 0.1 mg
10-663-45517 Measles Virus Non-Structural C-Protein (MEVNSCP) - Protein P; Non-structural protein C. 38 kDa_29 kDa N_A 0.5 mg
SCH-MCA4688 MOUSE ANTI INFLUENZA A NON STRUCTURAL PROTEIN , Product Type Monoclonal Antibody, Specificity INFLUENZA A NON STRUCTURAL PROTEIN, Target Species Viral, Host Mouse, Format Purified, Isotypes IgG2 0.2 mg
MCA4688 MOUSE ANTI INFLUENZA A NON STRUCTURAL PROTEIN , Product Type Monoclonal Antibody, Specificity INFLUENZA A NON STRUCTURAL PROTEIN, Target Species Viral, Host Mouse, Format Purified, Isotypes IgG2 0.2 mg
OBT1772 SMC2 (Structural Maintenance of Chromosomes 2), SMC2L1 (Structural Maintenance of Chromosomes 2_like 1), CAPE, CAP_E, hCAP_E (Human Chromosome _Associated Protein E), Rabbit anti_Human; WB 0.1 mg.
OBT1773 SMC2 (Structural Maintenance of Chromosomes 2), SMC2L1 (Structural Maintenance of Chromosomes 2_like 1), CAPE, CAP_E, hCAP_E (Human Chromosome _Associated Protein E), Rabbit anti_Human, Mouse; WB 0.1 mg.
OBT1774 SMC2 (Structural Maintenance of Chromosomes 2), SMC2L1 (Structural Maintenance of Chromosomes 2_like 1), CAPE, CAP_E, hCAP_E (Human Chromosome _Associated Protein E), Rabbit anti_Human, Mouse; WB_IP_I 0.1 mg.
OBT1774 SMC2 (Structural Maintenance of Chromosomes 2), SMC2L1 (Structural Maintenance of Chromosomes 2_like 1), CAPE, CAP_E, hCAP_E (Human Chromosome _Associated Protein E), Rabbit anti_Human, Mouse; WB_IP_I 0.1 mg.
25-030 ZC3H7B is a protein that contains a tetratricopeptide repeat domain. The encoded protein also interacts with the rotavirus non-structural protein NSP3. This gene encodes a protein that contains a tetr 0.05 mg
20-272-190412 Filensin - Mouse monoclonal [FIL - 7B10] to Filensin; Beaded filament structural protein 1; Lens fiber cell beaded-filament structural protein CP 115; CP115; Lens intermediate filament-like heavy; LIF 0.1 ml
27-617 ZC3H7B is a protein that contains a tetratricopeptide repeat domain. The encoded protein also interacts with the rotavirus non-structural protein NSP3. 0.1 mg
10-663-45516 Measles Virus Large structural Protein RNA Polymerase - Protein L; Transcriptase; Replicase N_A 0.1 mg
10-663-45516 Measles Virus Large structural Protein RNA Polymerase - Protein L; Transcriptase; Replicase N_A 0.5 mg
10-663-45516 Measles Virus Large structural Protein RNA Polymerase - Protein L; Transcriptase; Replicase N_A 1 mg
EIAAB38762 Cape,Chromosome-associated protein E,FGF-inducible protein 16,Fin16,Mouse,Mus musculus,SMC protein 2,Smc2,SMC-2,Smc2l1,Structural maintenance of chromosomes protein 2,XCAP-E homolog
26-812 LPP may play a structural role at sites of cell adhesion in maintaining cell shape and motility. In addition to these structural functions, it may also be implicated in signaling events and activation 0.05 mg
EIAAB38770 Kiaa0594,MLZ-453,Mouse,mSMC5,Mus musculus,Protein expressed in male leptotene and zygotene spermatocytes 453,SMC protein 5,Smc5,SMC-5,Smc5l1,Structural maintenance of chromosomes protein 5
EIAAB38761 CAPE,Chromosome-associated protein E,hCAP-E,Homo sapiens,Human,PRO0324,SMC protein 2,SMC2,SMC-2,SMC2L1,Structural maintenance of chromosomes protein 2,XCAP-E homolog
EIAAB38757 Rat,Rattus norvegicus,SMC protein 1A,Smc1,Smc1a,SMC-1A,Smc1l1,Structural maintenance of chromosomes protein 1A
EIAAB38758 Mouse,Mus musculus,SMC protein 1B,Smc1b,SMC-1B,SMC-1-beta,Smc1l2,Structural maintenance of chromosomes protein 1B
EIAAB38754 Bos taurus,Bovine,SMC protein 1A,SMC1,SMC1A,SMC-1A,SMC1L1,Structural maintenance of chromosomes protein 1A
orb81767 Measles Virus Non-Structural C-Protein (1-51) protein Proteins 100
EIAAB38772 Homo sapiens,hSMC6,Human,SMC protein 6,SMC6,SMC-6,SMC6L1,Structural maintenance of chromosomes protein 6


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur